7dtk | pdb_00007dtk
Crystal structure of the RecA1 domain of RNA helicase CGH-1 in C. elegans
Structural highlights
FunctionCGH1_CAEEL Probable RNA helicase required for oocyte and sperm function. Also required to prevent the physiological germline apoptosis mechanism killing essentially all developing oocytes.[1] [2] Publication Abstract from PubMedA protein-RNA complex containing the RNA helicase CGH-1 and a germline specific RNA-binding protein CAR-1 is involved in various aspects of function in C. elegans. However, the structural basis for the assembly of this protein complex remains unclear. Here, we elucidate the molecular basis of the recognition of CGH-1 by CAR-1. Additionally, we found that the ATPase activity of CGH-1 is stimulated by NTL-1a MIF4G domain in vitro. Furthermore, we determined the structures of the two RecA-like domains of CGH-1 by X-ray crystallography at resolutions of 1.85 and 2.40 A, respectively. Structural and biochemical approaches revealed a bipartite interface between CGH-1 RecA2 and the FDF-TFG motif of CAR-1. NMR and structure-based mutations in CGH-1 RecA2 or CAR-1 attenuated or disrupted CGH-1 binding to CAR-1, assessed by ITC and GST-pulldown in vitro. These findings provide insights into a conserved mechanism in the recognition of CGH-1 by CAR-1. Together, our data provide the missing physical links in understanding the assembly and function of CGH-1 and CAR-1 in C. elegans. Structural and biochemical insights into the recognition of RNA helicase CGH-1 by CAR-1 in C. elegans.,Zhang Y, Lv M, Li F, Li M, Zhang J, Shi Y, Hong J Biochem Biophys Res Commun. 2021 Mar 3;549:135-142. doi:, 10.1016/j.bbrc.2021.02.119. PMID:33676181[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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